Influenza virus A/USSR/90/77 variants adapted to mouse blood serum (USSR/90-MS) and lungs (USSR/90-ML) resistant to beta-inhibitors of mouse serum differ by biological properties and hemagglutinin (HA) structure. One of glycosylation site (GS) located at the tip of HA spike near the receptor binding site is lost because of mutations in both variants: GS 158 (Asn158Asp substitution) in USSR/90-MS and GS131 (Asp131Asp substitution) in USSR/90-ML. Probably adaptation to mouse lungs and serum represents adaptation to different types of receptor molecules. From these data we conclude that mouse lungs and/or bronchi and serum contain different beta-like inhibitors. Presumably the inhibitors in the lungs contain some additional factors in comparison with the serum, adaptation to which allows a wider spectrum of virus resistance to homologous and to many other normal animal sera.
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